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Database: UniProt
Entry: A0A151BG20_9ARCH
LinkDB: A0A151BG20_9ARCH
Original site: A0A151BG20_9ARCH 
ID   A0A151BG20_9ARCH        Unreviewed;       256 AA.
AC   A0A151BG20;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Type II methyltransferase {ECO:0000256|RuleBase:RU362026};
DE            EC=2.1.1.113 {ECO:0000256|RuleBase:RU362026};
DE   AltName: Full=N-4 cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU362026};
DE   Flags: Fragment;
GN   ORFNames=AYL31_010660 {ECO:0000313|EMBL:KYH38831.1};
OS   Candidatus Bathyarchaeota archaeon B26-1.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1779370 {ECO:0000313|EMBL:KYH38831.1, ECO:0000313|Proteomes:UP000075365};
RN   [1] {ECO:0000313|EMBL:KYH38831.1, ECO:0000313|Proteomes:UP000075365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B26-1 {ECO:0000313|EMBL:KYH38831.1};
RA   He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT   "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT   phylum Bathyarchaeota widespread in marine sediments.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000256|RuleBase:RU362026};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU362026}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYH38831.1}.
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DR   EMBL; LUCD01000103; KYH38831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BG20; -.
DR   STRING; 1779370.AYL31_010660; -.
DR   Proteomes; UP000075365; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU362026};
KW   Restriction system {ECO:0000256|RuleBase:RU362026};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU362026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          50..246
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
FT   NON_TER         256
FT                   /evidence="ECO:0000313|EMBL:KYH38831.1"
SQ   SEQUENCE   256 AA;  29627 MW;  E6CA7491FEDE7A83 CRC64;
     MKELRRSPSR PLQPRSNREG EKTVKVLRID DSHIVIFDDF RNVELDEKAD LVFADPPFGI
     GFKGNLQTYH RTPDALSYVE VPKEEYPDFI RSLLEWSYNV LKDSGSMWLL SGWNNLRVVL
     DAVEDAGFTQ INHCIWKYQF GVFTRRRFTT SHYHLLLLAK DPNNYTFNKP EHYAEDVWYI
     KRPYRHGVET AGNELPDELV EKCIRTSSNK GDLVVDPVLG SGTTMRVCLK TGRRCIGIEI
     NPALEKRIKQ KLGLNP
//
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